ID   F2R410_STRVP            Unreviewed;       564 AA.
AC   F2R410;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN   OrderedLocusNames=SVEN_5096 {ECO:0000313|EMBL:CCA58382.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58382.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA58382.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA58382.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR845719; CCA58382.1; -; Genomic_DNA.
DR   RefSeq; WP_015036280.1; NZ_JABVZO010000198.1.
DR   AlphaFoldDB; F2R410; -.
DR   SMR; F2R410; -.
DR   STRING; 953739.SVEN_5096; -.
DR   GeneID; 69867163; -.
DR   KEGG; sve:SVEN_5096; -.
DR   PATRIC; fig|953739.5.peg.233; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   OrthoDB; 9043248at2; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CCA58382.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   DOMAIN          31..433
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   564 AA;  64947 MW;  9D2D1C1AC0533F34 CRC64;
     MTVNEPVPDT FEDTPAKDLD PDWFKRAVFY EVLVRSFQDS NGDGVGDLKG ITSKLDYLQW
     LGVDCLWLPP FFKSPLRDGG YDVADYTSVL PEFGDLADFV EFVDAAHQRG MRVVIDFVMN
     HTSDQHEWFQ ESRRDPEGPY GDYYVWADDD KQYADARIIF VDTESSNWTF DPVRKQYYWH
     RFFSHQPDLN YENPAVQEEI LSALKFWLDL GIDGFRLDAV PYLYQQEGTN CENLPATHAF
     LKRVRKEIDD HYPDTVLLAE ANQWPEDVVD YFGDFRSGGD ECHMAFHFPV MPRIFMAVRR
     ESRYPVSEIL AKTPEIPSGC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
     IRRRLAPLLD NDRKQMELFT ALLFSLPGSP VLYYGDEIGM GDNIWLGDRD GVRTPMQWTP
     DRNAGFSSCD PGRLYLPAIM DPVHGYQVTN VEAGMASPSS LLHWTKRMIE IRKQNRAFGT
     GTYTELPASN PAVLAFLRED GDDLVLCVNN FSRFAQPTEL DLRRFDGTQP VELIGGVTFP
     AIGQLPYLLT LAGHGFYWFR LKKG
//